Cloned (Comment) | Organism |
---|---|
truncated protein lacking the C-terminal domain is expressed | Homo sapiens |
Protein Variants | Comment | Organism |
---|---|---|
DELTAC | studies are carried out using a truncated protein lacking the C-terminal domain. kcat increases by a factor of 4 and the responsiveness to S-adenosyl-L-methionine is lost. The C-terminal domain is involved in the aggregation of the full-length protein, which exists as a mixture of tetramer and higher oligomers, while the 45 kDa truncated form lacking the C-terminal domain is a dimer | Homo sapiens |
R266M | enzyme is inactivated, pyridoxal 5'-phosphate is displaced by breaking the salt bridge between Cys52 and Arg266 | Homo sapiens |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
CO | CO binding is found to induce a tautomeric shift of the pyridoxal 5'-phosphate from the ketoenamine to the enolimine form. The ketoenamine is key to pyridoxal 5'-phosphate reactivity because its imine C-N bond is protonated, facilitating attack by the nucleophilic substrate, serine | Homo sapiens | |
NO | - |
Homo sapiens |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
45000 | - |
molecular weight of the truncated protein lacking the C-terminal domain | Homo sapiens |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Subunits | Comment | Organism |
---|---|---|
dimer | - |
Homo sapiens |
Synonyms | Comment | Organism |
---|---|---|
CBS | - |
Homo sapiens |
cystathionine beta-synthase | - |
Homo sapiens |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
heme | CO binding displaces Cys52 from the heme | Homo sapiens | |
pyridoxal 5'-phosphate | - |
Homo sapiens |